Journal
INORGANIC CHEMISTRY
Volume 51, Issue 3, Pages 1210-1212Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ic2023314
Keywords
-
Categories
Funding
- Swiss National Science Foundation [PZ00P2_121989]
- Swiss National Science Foundation (SNF) [PZ00P2_121989] Funding Source: Swiss National Science Foundation (SNF)
Ask authors/readers for more resources
The reactivity of the [Re(CO)(3)(H2O)(2)](+) complex coordinated to the His15 residue of HEW lysozyme is described. In the fully metalated protein (Lys-1), the Re ion retains its reactivity only toward selected ligands, while others induce a ligand-mediated demetalation of the enzyme. It is further shown that some of the complexes that may be engineered on the lysozyme do not react with the free protein even if present in solution in excess. The formation of stable metal adducts starting from Lys-1 was confirmed by X-ray crystallography.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available